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Structure of a robust bacterial protein cage and its application as a versatile biocatalytic platform through enzyme encapsulation
- Source :
- Biochemical and biophysical research communications 529(3), 548-553 (2020). doi:10.1016/j.bbrc.2020.06.059, Biochemical and Biophysical Research Communications, 529(3):j.bbrc.2020.06.059, 548-553. ACADEMIC PRESS INC ELSEVIER SCIENCE
- Publication Year :
- 2020
- Publisher :
- Academic Press, 2020.
-
Abstract
- Biochemical and biophysical research communications 529(3), 548 - 553 (2020). doi:10.1016/j.bbrc.2020.06.059<br />Using a newly discovered encapsulin from Mycolicibacterium hassiacum, several biocatalysts were packaged in this robust protein cage. The encapsulin was found to be easy to produce as recombinant protein. Elucidation of its crystal structure revealed that it is a spherical protein cage of 60 protomers (diameter of 23 nm) with narrow pores. By developing an effective coexpression and isolation procedure, the effect of packaging a variety of biocatalysts could be evaluated. It was shown that encapsulation results in a significantly higher stability of the biocatalysts. Most of the targeted cofactor-containing biocatalysts remained active in the encapsulin. Due to the restricted diameters of the encapsulin pores (5–9 Å), the protein cage protects the encapsulated enzymes from bulky compounds. The work shows that encapsulins may be valuable tools to tune the properties of biocatalysts such as stability and substrate specificity.<br />Published by Academic Press, Orlando, Fla.
- Subjects :
- 0301 basic medicine
THERMOBIFIDA-FUSCA
Encapsulin
Biophysics
Nanoparticle
Protein cage
OXIDASE
Crystallography, X-Ray
Biochemistry
Substrate Specificity
Bacterial protein
03 medical and health sciences
0302 clinical medicine
Bacterial Proteins
Microscopy, Electron, Transmission
ddc:570
Enzyme Stability
NANOPARTICLES
Molecular Biology
Mycobacteriaceae
IN-VIVO
Thermobifida fusca
NANOCOMPARTMENT
Cofactor
Chemistry
Crystal structure
Cryoelectron Microscopy
PEROXIDASE
Temperature
Cell Biology
Enzymes, Immobilized
equipment and supplies
Combinatorial chemistry
Enzyme encapsulation
Recombinant Proteins
Enzymes
030104 developmental biology
Biocatalysis
030220 oncology & carcinogenesis
Substrate specificity
Cage
Subjects
Details
- Language :
- English
- ISSN :
- 0006291X
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications 529(3), 548-553 (2020). doi:10.1016/j.bbrc.2020.06.059, Biochemical and Biophysical Research Communications, 529(3):j.bbrc.2020.06.059, 548-553. ACADEMIC PRESS INC ELSEVIER SCIENCE
- Accession number :
- edsair.doi.dedup.....e2e6f8b1051cf92387af9dc029f32004